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Database: UniProt
Entry: A0A059BT21_EUCGR
LinkDB: A0A059BT21_EUCGR
Original site: A0A059BT21_EUCGR 
ID   A0A059BT21_EUCGR        Unreviewed;       790 AA.
AC   A0A059BT21;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=EUGRSUZ_F02760 {ECO:0000313|EMBL:KCW69257.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW69257.1};
RN   [1] {ECO:0000313|EMBL:KCW69257.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW69257.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC       subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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DR   EMBL; KK198758; KCW69257.1; -; Genomic_DNA.
DR   RefSeq; XP_010062183.1; XM_010063881.1.
DR   AlphaFoldDB; A0A059BT21; -.
DR   EnsemblPlants; KCW69257; KCW69257; EUGRSUZ_F02760.
DR   Gramene; KCW69257; KCW69257; EUGRSUZ_F02760.
DR   OrthoDB; 5475716at2759; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17959; DEADc_DDX54; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR012541; DBP10_C.
DR   InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR   Pfam; PF08147; DBP10CT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01123; DBP10CT; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          28..56
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          59..232
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          256..405
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           28..56
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        11..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..771
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..790
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  88951 MW;  3D720CC648AB1552 CRC64;
     MAGGVHPYVS SKAELKRREQ QRKKARSGGF ESLGLSPDVF RGVKRKGYRV PTPIQRKTMP
     LILSGADVVA MARTGSGKTA AFLVPMLERL KQHLPQGGVR ALILSPTRDL ALQTLKFTKE
     LGRFTDLRTS LLVGGDSMES QFEELAQNPD IIIATPGRLM HHLSEVDDMT LRTVEYVVFD
     EADCLFGMGF AEQLHKILSQ LSENRQTLLF SATLPSALAE FAKAGLRDPQ LVRLDLETRI
     SPDLKLAFFT LRQEEKHAAL LYLIREQISS DQQTLIFVST KHHVEFLNSL FREEGIEPSV
     CYGDMDQDAR KIHVSRFRSR KTMLLIVTDV AARGIDIPLL DNVINWDFPP KPKIFVHRVG
     RAARAGRTGT AYSFMTTEDM AYLLDLHLFL SKPIWPAPTE DEVLKDMDGV MSKIDQAIAN
     GETVYGRFPQ TVIDLVSDRV REIIDSSAEL YALQKTCTNA FRLYSKTKPS PSKESIRRVK
     DLPREGLHPL FRNVLAGGEL VALAFSERLK TFRPKQTILE AEGEAAKSKH VQGPSCQWVD
     VMKKKRAIHD GIINLVQQQK HDSKPSEEVE INPVSTSSKE KETKARGSKR KSRNFKDDEY
     YISSIPTNHH MESGLAVRAN EGFGSNRLES AVLDLVADDS GGIRKQRSSY HWDKRSKKYV
     KLNNGERVTA SGKIKTESGA KVKANKTGIY KKWKERSHSK ISLKGTSNEE NSVESAGMAG
     DRKFQRTNRK FKGGYKQRSL PNANIRSEIK NLEQVRKERQ KKADRISYMK SKSAKSKKLG
     KNGKKRKGKK
//
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